ACL_RS06655

Uniprot: A9NHV7
Description: HPr(Ser) kinase/phosphatase
EC number: 2.7.11.-; 2.7.4.-
Annotation score: 4 out of 5
Miscellaneous [CC]: MISCELLANEOUS: Both phosphorylation and phosphorolysis are carried out by the same active site and suggest a common mechanism for both reactions. {ECO:0000256|HAMAP-Rule:MF_01249}.
Protein existence: Inferred from homology
Catalytic activity: CATALYTIC ACTIVITY: ATP + HPr = ADP + P-Ser-HPr. {ECO:0000256|HAMAP-Rule:MF_01249, ECO:0000256|SAAS:SAAS00281214}.; CATALYTIC ACTIVITY: P-Ser-HPr + phosphate = HPr + diphosphate. {ECO:0000256|HAMAP-Rule:MF_01249, ECO:0000256|SAAS:SAAS00281211}.
Cofactor: COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-Rule:MF_01249, ECO:0000256|SAAS:SAAS00281221};
Enzyme regulation:
Function [CC]: FUNCTION: Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr). {ECO:0000256|HAMAP-Rule:MF_01249}.
Pathway:
Active site: ACT_SITE 141 141 {ECO:0000256|HAMAP-Rule:MF_01249}.; ACT_SITE 162 162 {ECO:0000256|HAMAP-Rule:MF_01249}.; ACT_SITE 180 180 Proton acceptor; for phosphorylation activity. Proton donor; for dephosphorylation activity. {ECO:0000256|HAMAP-Rule:MF_01249}.; ACT_SITE 246 246 {ECO:0000256|HAMAP-Rule:MF_01249}.
Binding site:
Calcium binding:
DNA binding:
Metal binding: METAL 163 163 Magnesium. {ECO:0000256|HAMAP-Rule:MF_01249}.; METAL 205 205 Magnesium. {ECO:0000256|HAMAP-Rule:MF_01249}.
Nucleotide binding: NP_BIND 156 163 ATP. {ECO:0000256|HAMAP-Rule:MF_01249}.
Site:
Gene names (primary): hprK
Gene names (synonym):
Mass: 35,484
Subunit structure [CC]: SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_01249, ECO:0000256|SAAS:SAAS00281210}.
Gene ontology (GO): intracellular [GO:0005622]; ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; phosphorelay sensor kinase activity [GO:0000155]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; regulation of carbohydrate metabolic process [GO:0006109]
Gene ontology IDs: GO:0000155; GO:0000287; GO:0004674; GO:0004712; GO:0005524; GO:0005622; GO:0006109
Chain:
Signal peptide:
Domain [CC]: DOMAIN: The Walker A ATP-binding motif also binds Pi and PPi. {ECO:0000256|HAMAP-Rule:MF_01249}.
Sequence similarities: SIMILARITY: Belongs to the HPrK/P family. {ECO:0000256|HAMAP-Rule:MF_01249, ECO:0000256|SAAS:SAAS00535415}.
Protein families: HPrK/P family
Coiled coil:
Domain [FT]: DOMAIN 7 130 Hpr_kinase_N. {ECO:0000259|Pfam:PF02603}.; DOMAIN 133 301 Hpr_kinase_C. {ECO:0000259|Pfam:PF07475}.
Motif:
Region: REGION 204 213 Important for the catalytic mechanism of both phosphorylation and dephosphorylation. {ECO:0000256|HAMAP-Rule:MF_01249}.; REGION 267 272 Important for the catalytic mechanism of dephosphorylation. {ECO:0000256|HAMAP-Rule:MF_01249}.
EMBL: CP000896
ProteinModelPortal: A9NHV7
MEROPS:
EnsemblBacteria KO: ABX81937
UniPathway: K06023
CDD:
Gene3D:
HAMAP: 3.40.1390.20;3.40.50.300
InterPro: MF_01249
PANTHER: IPR003755;IPR011104;IPR011126;IPR027417;IPR028979
PIRSF:
PRINTS:
PROSITE:
Pfam:
ProDom: PF07475;PF02603
SMART:
SUPFAM:
TIGRFAMs: SSF75138

1403636-1404590(-)

>nucleotide sequence
TTAAATGTCGTCATCATCGTCTTCTGCTCCTTTTGCAGCTTTTGCTGCTACGTTTTGTAT
AAGTGTTTCTGCTGCGTTATAACCTAAATATTTTAACTTTTGATTCATTGCTGCAGATTC
TACTAGGGTTGCGTTATTACGTCCTGGTAAAACTGGAATCGTAATCTTTGGTATTTCGGT
ACCAAAAATAGTATAGTTTTGAGTTTCAATACCTAGTCGGTCATAAGTTTTAGACTTATC
CCAATGTTCTAATTCAATCACTAATCTAATTTTTTTGTTTTCTCTAAATGCTCCAGCACC
TAACATTTGAACCACATCTACAATACCAATACCGCGTATTTCTATATAGCGCTCTAGTAT
TTTTGGTGCTTGACCAATAATCACACCTGGAGCTGTTTCATAAACATCCACTCGATCATC
AGCAACTAAAATATGATTTCTTTTAATCAGTTCCAGAGCAGTTTCAGATTTACCTACACC
GGATTTACCAATAATTAATGTACCCATGCCATAAATATCTAGTAACGTACCATGAATACT
TTCACGTGGTGCAAGTGCACTACGTAAATAAGAATATAGTTTTGAGTTAATTGGTGTTGT
ACGTTCATTGGATTTATAAAGTGGTACATGATACTTATTACCTAAGTCCATAAAGTATTG
TGGGATATCCACATTAATACTAAATATCACTGCAGGTGGTTGTAGTTTAAGTACTGCATC
TACACGCTCAATTTGAACTTGTTCATCTAGTAACATCAAAAAGTGTGCTTCTTTTGAACC
GATAAGTAAAATACGTTGTGGATCAAAAAAGTCTAAGAATCCAGCAAACTCAACACCGGG
TCTGCTAAGCATTTCTACTTCTACACGTCTATCCTCTCCGTCAAAACCTGCCACTATTTT
TAAATTTAAGTCATGTGCTATTTTTTTAAGTCTAATTGAATTTTTATAAGCCAT

>protein sequence
MAYKNSIRLKKIAHDLNLKIVAGFDGEDRRVEVEMLSRPGVEFAGFLDFFDPQRILLIGS
KEAHFLMLLDEQVQIERVDAVLKLQPPAVIFSINVDIPQYFMDLGNKYHVPLYKSNERTT
PINSKLYSYLRSALAPRESIHGTLLDIYGMGTLIIGKSGVGKSETALELIKRNHILVADD
RVDVYETAPGVIIGQAPKILERYIEIRGIGIVDVVQMLGAGAFRENKKIRLVIELEHWDK
SKTYDRLGIETQNYTIFGTEIPKITIPVLPGRNNATLVESAAMNQKLKYLGYNAAETLIQ
NVAAKAAKGAEDDDDDI